Segmented cells selectins

These interactions involve adhesion proteins called selectins, which are found both on the rolling leukocytes and on the endothelial cells of the vascular walls. Selectins have a characteristic domain structure, consisting of an N-terminal extracellular lectin domain, a single epidermal growth factor (EGR) domain, a series of two to nine short consensus repeat (SCR) domains, a single transmembrane segment, and a short cytoplasmic domain. Lectin domains, first characterized in plants, bind carbohydrates... 

Selectins are cell-adhesion molecules that mediate leukocyte recruitment in irmnune reactions and signal transduction. Selectins comprise three members termed E-, P-, and L-selectin. The CRD is located at the N-terminus, followed by an EGF-hke domain. There are various numbers of consensus repeat sequences following the EGF-like domain. P-selectin, L-selectin and E-selectin contain nine, six, and two repeats, respectively. A transmembrane segment and a cytoplasmic tail are located at the C-terminal. The key domains for target recognition and sugar binding are the N-terminal CRD and EGF-like domain. ... 

Sako, D, Comess, K M, Barone, K M, Camphausen, R T, Cumming, D A, Shaw, G D, A suffated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell, 83, 323-331, 1995. 

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